MEPS_SHIFL
ID MEPS_SHIFL Reviewed; 188 AA.
AC P0AFV7; O08016; P77685;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Murein DD-endopeptidase MepS/Murein LD-carboxypeptidase;
DE EC=3.4.-.-;
DE EC=3.4.17.13;
DE AltName: Full=Lipoprotein Spr;
DE AltName: Full=Murein hydrolase MepS;
DE Flags: Precursor;
GN Name=mepS; Synonyms=spr; OrderedLocusNames=SF2262, S2391;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: A murein DD-endopeptidase with specificity for D-Ala-meso-
CC diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave
CC D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell
CC wall expansion. Functionally redundant with MepM and MepH. Also has
CC weak LD-carboxypeptidase activity on L-mDAP-D-Ala peptide bonds (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-
CC glutamyl-6-carboxy-L-lysyl-D-alanine = D-alanine + N-acetyl-D-
CC glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl;
CC Xref=Rhea:RHEA:48688, ChEBI:CHEBI:15377, ChEBI:CHEBI:57416,
CC ChEBI:CHEBI:90762, ChEBI:CHEBI:90763; EC=3.4.17.13;
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01284, ECO:0000305}.
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DR EMBL; AE005674; AAN43781.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17598.1; -; Genomic_DNA.
DR RefSeq; NP_708074.1; NC_004337.2.
DR RefSeq; WP_000241011.1; NZ_WPGW01000022.1.
DR AlphaFoldDB; P0AFV7; -.
DR BMRB; P0AFV7; -.
DR SMR; P0AFV7; -.
DR STRING; 198214.SF2262; -.
DR MEROPS; C40.004; -.
DR EnsemblBacteria; AAN43781; AAN43781; SF2262.
DR EnsemblBacteria; AAP17598; AAP17598; S2391.
DR GeneID; 1027294; -.
DR GeneID; 67414541; -.
DR KEGG; sfl:SF2262; -.
DR KEGG; sfx:S2391; -.
DR PATRIC; fig|198214.7.peg.2711; -.
DR HOGENOM; CLU_016043_9_1_6; -.
DR OMA; MHAVNDK; -.
DR OrthoDB; 682655at2; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0106415; F:muramoyltetrapeptide carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF00877; NLPC_P60; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Hydrolase; Lipoprotein; Membrane; Palmitate; Protease;
KW Reference proteome; Signal; Thiol protease.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 27..188
FT /note="Murein DD-endopeptidase MepS/Murein LD-
FT carboxypeptidase"
FT /id="PRO_0000045243"
FT DOMAIN 64..185
FT /note="NlpC/P60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 94
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT LIPID 27
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 27
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 188 AA; 21040 MW; 65DCEEDBDDC76098 CRC64;
MVKSQPILRY ILRGIPAIAV AVLLSACSAN NTAKNMHPET RAVGSETSSL QASQDEFENL
VRNVDVKSRI MDQYADWKGV RYRLGGSTKK GIDCSGFVQR TFREQFGLEL PRSTYEQQEM
GKSVSRSNLR TGDLVLFRAG STGRHVGIYI GNNQFVHAST SSGVIISSMN EPYWKKRYNE
ARRVLSRS
